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Email: info@nsjbio.com
- Tel: 858.663.9055
- Email: info@nsjbio.com
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Alpha A Crystallin Antibody / Molecular Chaperone Antibody recognizes Alpha A Crystallin (CRYAA), a major structural protein of the vertebrate eye lens and a member of the small heat shock protein family. Alpha A Crystallin functions as an ATP-independent molecular chaperone that binds partially unfolded proteins, preventing their aggregation and preserving lens transparency throughout development and aging. As one of the most abundant proteins in lens fiber cells, it is essential for maintaining optical clarity, protein stability, and long-term lens integrity. In addition to its structural role, Alpha A Crystallin protects cells from oxidative stress, apoptosis, and protein misfolding, making it a critical regulator of protein homeostasis and cellular survival. Because of its conserved chaperone activity and abundant expression within the lens, Alpha A Crystallin is widely used as a marker of lens differentiation, ocular development, and cataract research.
Although predominantly associated with the eye, Alpha A Crystallin is also expressed in the retina, skeletal muscle, heart, brain, and several epithelial tissues, where it performs important cytoprotective functions. As a molecular chaperone, CRYAA stabilizes damaged proteins, reduces protein aggregation, and supports proper protein folding during oxidative stress, heat shock, inflammation, and other cellular insults. These activities help preserve mitochondrial function, inhibit apoptosis, and promote cell survival under adverse physiological conditions. Consequently, Alpha A Crystallin has become an important marker for studies of protein quality control, stress adaptation, neuroprotection, and tissue regeneration.
Mutations in the CRYAA gene are a well-established cause of congenital cataracts and have also been linked to age-related cataracts, microphthalmia, and additional inherited ocular disorders. Altered Alpha A Crystallin expression has further been associated with retinal degeneration, glaucoma, cardiovascular disease, and several human cancers, where dysregulated chaperone activity can influence cellular proliferation, migration, therapeutic resistance, and survival. Growing evidence indicates that Alpha A Crystallin contributes to maintenance of stem cell viability and protection against neurodegenerative processes, expanding its importance beyond ophthalmic research into neuroscience and regenerative medicine.
Alpha A Crystallin Antibody / Molecular Chaperone Antibody is an excellent tool for investigations of lens biology, molecular chaperone function, protein homeostasis, oxidative stress, apoptosis, neuroprotection, cataract mechanisms, and ocular disease. Researchers also use Alpha A Crystallin Antibody / Molecular Chaperone Antibody to study cellular stress responses, tissue regeneration, protein quality control, and diseases characterized by protein aggregation. Its diverse biological functions and highly conserved expression make Alpha A Crystallin an important biomarker for both basic and translational biomedical research.
Explore our Cell Biology Antibodies page to learn more about proteins that regulate molecular chaperone activity, protein homeostasis, cellular stress responses, and protein quality control.
Optimal dilution of the Alpha A Crystallin Antibody / Molecular Chaperone Antibody should be determined by the researcher.
Amino acids M1-S173 from the human protein were used as the immunogen for the Alpha A Crystallin antibody.
After reconstitution, the Alpha A Crystallin antibody can be stored for up to one month at 4oC. For long-term, aliquot and store at -20oC. Avoid repeated freezing and thawing.
Alpha A Crystallin antibody, CRYAA antibody, Alpha Crystallin A antibody, Crystallin Alpha A antibody, Lens Structural Protein antibody, Small Heat Shock Protein antibody
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